Antimicrobial peptide epinecidin-1 modulates MyD88 protein levels via the proteasome degradation pathway

Bor Chyuan Su, Jyh Yih Chen

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)


The cationic antimicrobial peptide epinecidin-1 was identified from Epinephelus coioides and possesses multiple biological functions, including antibacterial, antifungal, anti-tumor, and immunomodulatory effects. In addition, epinecidin-1 suppresses lipopolysaccharide (LPS)-induced inflammation by neutralizing LPS and ameliorating LPS/Toll-like receptor (TLR)-4 internalization. However, it is unclear whether the actions of epinecidin-1 depend on the regulation of TLR adaptor protein MyD88 or endogenous TLR signaling antagonists, which include A20, interleukin-1 receptor associated kinase (IRAK)-M, and suppressor of cytokine signaling (SOCS)-1. Our results demonstrate that epinecidin-1 alone does not affect A20, IRAK-M, or SOCS-1 protein levels. However, pre-incubation of epinecidin-1 significantly inhibits LPS-induced upregulation of A20, IRAK-M, and SOCS-1. In addition, epinecidin-1 significantly reduces the abundance of MyD88 protein. Both MG132 (a specific proteasome inhibitor) and Heclin (a specific Smurf E3 ligase inhibitor) are able to abolish epinecidin-1-mediated MyD88 degradation. Thus, our data suggest that epinecidin-1 directly inhibits MyD88 via induction of the Smurf E3 ligase proteasome pathway.

Original languageEnglish
Article number362
JournalMarine Drugs
Issue number11
Publication statusPublished - Nov 1 2017
Externally publishedYes


  • A20
  • Epinecidin-1
  • IRAK-M
  • MyD88
  • Proteasome
  • SOCS-1

ASJC Scopus subject areas

  • Drug Discovery


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